Since the first pioneering studies on small deuterated peptides dating more than 20 years
ago, 1H detection has evolved into the most efficient approach for investigation of …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for
analyzing protein structure, interaction, and dynamics at atomic resolution and in various …

Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has
focused on highly deuterated samples, in which only a small number of protons are …

Internuclear distances represent one of the main structural constraints in molecular structure
determination using solid-state NMR spectroscopy, complementing chemical shifts and …

Solid-state nuclear magnetic resonance (ssNMR) methods can probe the motions of
membrane proteins in liposomes at the atomic level and propel the understanding of …

Recently, proton-detected magic-angle spinning (MAS) solid-state nuclear magnetic
resonance (NMR) spectroscopy has become an attractive tool to study the structure and …

Proton detection developed in the last 20 years as the method of choice to study
biomolecules in the solid state. In perdeuterated proteins, proton dipolar interactions are …

We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid‐
state NMR spectroscopy with 100–111 kHz magic‐angle spinning (MAS). The excellent …

Solid-state nuclear magnetic resonance (SSNMR) spectroscopy elucidates membrane
protein structures and dynamics in atomic detail to yield mechanistic insights. By …